ID B7UGZ6_ECO27 Unreviewed; 475 AA.
AC B7UGZ6;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=qseE {ECO:0000313|EMBL:CAS10381.1};
GN OrderedLocusNames=E2348C_2833 {ECO:0000313|EMBL:CAS10381.1};
OS Escherichia coli O127:H6 (strain E2348/69 / EPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=574521 {ECO:0000313|EMBL:CAS10381.1, ECO:0000313|Proteomes:UP000008205};
RN [1] {ECO:0000313|EMBL:CAS10381.1, ECO:0000313|Proteomes:UP000008205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E2348/69 / EPEC {ECO:0000313|Proteomes:UP000008205};
RX PubMed=18952797; DOI=10.1128/JB.01238-08;
RA Iguchi A., Thomson N.R., Ogura Y., Saunders D., Ooka T., Henderson I.R.,
RA Harris D., Asadulghani M., Kurokawa K., Dean P., Kenny B., Quail M.A.,
RA Thurston S., Dougan G., Hayashi T., Parkhill J., Frankel G.;
RT "Complete genome sequence and comparative genome analysis of
RT enteropathogenic Escherichia coli O127:H6 strain E2348/69.";
RL J. Bacteriol. 191:347-354(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}.
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DR EMBL; FM180568; CAS10381.1; -; Genomic_DNA.
DR RefSeq; WP_001297612.1; NC_011601.1.
DR AlphaFoldDB; B7UGZ6; -.
DR SMR; B7UGZ6; -.
DR GeneID; 75206249; -.
DR KEGG; ecg:E2348C_2833; -.
DR HOGENOM; CLU_000445_89_23_6; -.
DR Proteomes; UP000008205; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR PANTHER; PTHR43711:SF31; SENSOR HISTIDINE KINASE GRAS; 1.
DR PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:CAS10381.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000008205};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 174..198
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 256..472
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 475 AA; 53307 MW; 00B826F763BBF090 CRC64;
MKRWPVFPRS LRQLVMLAFL LILLPLLVLA WQAWQSLNAL SDQAALVNRT TLIDARRSEA
MTNAALEMER SYRQYCVLDD PTLAKVYQSQ RKRYSEMLDA HAGVLPDDKL YQALRQDLNN
LAQLQCNNSG PDAAAAARLE AFASANTEMV QATRTVVFSR GQQLQREIAE RGQYFGWQSL
VLFLVSLVMV LLFTRMIIGP VKNIERMINR LGEGRSLGNS VSFSGPSELR SVGQRILWLS
ERLSWLESQR HQFLRHLSHE LKTPLASMRE GTELLADQVV GPLTPEQKEV VSILDSSSRN
LQKLIEQLLD YNRKQADSAV ELENVELAPL VETVVSAHSL PARAKMMHTD VDLKATACLA
EPMLLMSVLD NLYSNAVHYG AESGNICLRS SLHGARVYID VINTGTPIPQ EERAMIFEPF
FQGSHQRKGA VKGSGLGLSI ARDCIRRMQG ELYLVDESGQ DVCFRIELPS SKNTK
//
